LOCUS NP_777280 383 aa linear PRI 22-OCT-2008
DEFINITION isocitrate dehydrogenase 3, beta subunit isoform b precursor [Homo
sapiens].
ACCESSION NP_777280
VERSION NP_777280.1 GI:28178816
DBSOURCE REFSEQ: accession NM_174855.1
KEYWORDS .
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 383)
AUTHORS Hartong,D.T., Dange,M., McGee,T.L., Berson,E.L., Dryja,T.P. and
Colman,R.F.
TITLE Insights from retinitis pigmentosa into the roles of isocitrate
dehydrogenases in the Krebs cycle
JOURNAL Nat. Genet. 40 (10), 1230-1234 (2008)
PUBMED 18806796
REFERENCE 2 (residues 1 to 383)
AUTHORS Bzymek,K.P. and Colman,R.F.
TITLE Role of alpha-Asp181, beta-Asp192, and gamma-Asp190 in the
distinctive subunits of human NAD-specific isocitrate dehydrogenase
JOURNAL Biochemistry 46 (18), 5391-5397 (2007)
PUBMED 17432878
REMARK GeneRIF: Asp192 is needed for optimal affinity of IDH beta subunit
for nicotinamide-adenine dinucleotide (NAD) substrate, but is not
critical for catalysis.
REFERENCE 3 (residues 1 to 383)
AUTHORS Soundar,S., O'hagan,M., Fomulu,K.S. and Colman,R.F.
TITLE Identification of Mn2+-binding aspartates from alpha, beta, and
gamma subunits of human NAD-dependent isocitrate dehydrogenase
JOURNAL J. Biol. Chem. 281 (30), 21073-21081 (2006)
PUBMED 16737955
REMARK GeneRIF: active sites of the human NAD-IDH are shared between alpha
and gamma subunits and between alpha and beta subunits
REFERENCE 4 (residues 1 to 383)
AUTHORS Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
and Zoghbi,H.Y.
TITLE A protein-protein interaction network for human inherited ataxias
and disorders of Purkinje cell degeneration
JOURNAL Cell 125 (4), 801-814 (2006)
PUBMED 16713569
REFERENCE 5 (residues 1 to 383)
AUTHORS Kil,I.S. and Park,J.W.
TITLE Regulation of mitochondrial NADP+-dependent isocitrate
dehydrogenase activity by glutathionylation
JOURNAL J. Biol. Chem. 280 (11), 10846-10854 (2005)
PUBMED 15653693
REMARK GeneRIF: IDPm activity appears to be modulated through enzymatic
glutathionylation and deglutathionylation during oxidative stress
REFERENCE 6 (residues 1 to 383)
AUTHORS Soundar,S., Park,J.H., Huh,T.L. and Colman,R.F.
TITLE Evaluation by mutagenesis of the importance of 3 arginines in
alpha, beta, and gamma subunits of human NAD-dependent isocitrate
dehydrogenase
JOURNAL J. Biol. Chem. 278 (52), 52146-52153 (2003)
PUBMED 14555658
REFERENCE 7 (residues 1 to 383)
AUTHORS Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
Rogers,J.
TITLE The DNA sequence and comparative analysis of human chromosome 20
JOURNAL Nature 414 (6866), 865-871 (2001)
PUBMED 11780052
REFERENCE 8 (residues 1 to 383)
AUTHORS Weiss,C., Zeng,Y., Huang,J., Sobocka,M.B. and Rushbrook,J.I.
TITLE Bovine NAD+-dependent isocitrate dehydrogenase: alternative
splicing and tissue-dependent expression of subunit 1
JOURNAL Biochemistry 39 (7), 1807-1816 (2000)
PUBMED 10677231
REFERENCE 9 (residues 1 to 383)
AUTHORS Kim,Y.O., Koh,H.J., Kim,S.H., Jo,S.H., Huh,J.W., Jeong,K.S.,
Lee,I.J., Song,B.J. and Huh,T.L.
TITLE Identification and functional characterization of a novel,
tissue-specific NAD(+)-dependent isocitrate dehydrogenase beta
subunit isoform
JOURNAL J. Biol. Chem. 274 (52), 36866-36875 (1999)
PUBMED 10601238
REFERENCE 10 (residues 1 to 383)
AUTHORS Kim,Y.O., Park,S.H., Kang,Y.J., Koh,H.J., Kim,S.H., Park,S.Y.,
Sohn,U. and Huh,T.L.
TITLE Assignment of mitochondrial NAD(+)-specific isocitrate
dehydrogenase beta subunit gene (IDH3B) to human chromosome band
20p13 by in situ hybridization and radiation hybrid mapping
JOURNAL Cytogenet. Cell Genet. 86 (3-4), 240-241 (1999)
PUBMED 10575215
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AL049712.12 and BC001960.1.
Summary: Isocitrate dehydrogenases catalyze the oxidative
decarboxylation of isocitrate to 2-oxoglutarate. These enzymes
belong to two distinct subclasses, one of which utilizes NAD(+) as
the electron acceptor and the other NADP(+). Five isocitrate
dehydrogenases have been reported: three NAD(+)-dependent
isocitrate dehydrogenases, which localize to the mitochondrial
matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of
which is mitochondrial and the other predominantly cytosolic.
NAD(+)-dependent isocitrate dehydrogenases catalyze the
allosterically regulated rate-limiting step of the tricarboxylic
acid cycle. Each isozyme is a heterotetramer that is composed of
two alpha subunits, one beta subunit, and one gamma subunit. The
protein encoded by this gene is the beta subunit of one isozyme of
NAD(+)-dependent isocitrate dehydrogenase. Three alternatively
spliced transcript variants encoding different isoforms have been
described for this gene. [provided by RefSeq].
Transcript Variant: This variant (2) is also known as IDHB2. It
lacks a region in the coding region, which results in a frameshift
and an early stop codon, compared to variant 1. The encoded isoform
(b) is shorter and has a distinct C-terminus compared to isoform a.
FEATURES Location/Qualifiers
source 1..383
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="20"
/map="20p13"
Protein 1..383
/product="isocitrate dehydrogenase 3, beta subunit isoform
b precursor"
/EC_number="1.1.1.41"
/note="isocitric dehydrogenase; NAD+-specific isocitrate
dehydrogenase beta; NAD+-specific isocitrate dehydrogenase
b subunit; NAD+-specific ICDH; isocitrate dehydrogenase,
NAD(+)-specific, mitochondrial, beta subunit"
transit_peptide 1..34
/calculated_mol_wt=3408
mat_peptide 35..383
/product="isocitrate dehydrogenase 3, beta subunit isoform
b"
/calculated_mol_wt=38498
CDS 1..383
/gene="IDH3B"
/gene_synonym="H-IDHB"
/gene_synonym="MGC903"
/gene_synonym="FLJ11043"
/coded_by="NM_174855.1:10..1161"
/note="isoform b precursor is encoded by transcript
variant 2"
/db_xref="CCDS:CCDS13031.1"
/db_xref="GeneID:3420"
/db_xref="HGNC:5385"
/db_xref="MIM:604526"
ORIGIN
1 maalsgvrwl tralvsagnp gawrglstsa aahaasrsqa edvrvegsfp vtmlpgdgvg
61 pelmhavkev fkaaavpvef qehhlsevqn maseekleqv lssmkenkva iigkihtpme
121 ykgelasydm rlrrkldlfa nvvhvkslpg ymtrhnnldl viireqtege ysslehesar
181 gvieclkivt raksqriakf afdyatkkgr gkvtavhkan imklgdglfl qcceevaely
241 pkikfetmii dnccmqlvqn pyqfdvlvmp nlygniidnl aaglvggagv vpgesysaey
301 avfetgarhp faqavgrnia nptamllsas nmlrhlnley hssmiadavk kvikvgkvrt
361 sdmggyatch dfteaviaal php
//